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Volumn 26, Issue 12, 2005, Pages 2412-2426

Discovery of an MIT-like atracotoxin family: Spider venom peptides that share sequence homology but not pharmacological properties with AVIT family proteins

Author keywords

ACTX Hvf17; Bv8; Funnel web spider; Mamba intestinal toxin 1; Prokineticin

Indexed keywords

ATRACOTOXIN; DISULFIDE; ENDOCRINE GLAND DERIVED VASCULAR ENDOTHELIAL GROWTH FACTOR; MAMBA INTESTINAL TOXIN 1; PEPTIDE; SPIDER VENOM; TOXIN; UNCLASSIFIED DRUG;

EID: 27944491979     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2005.05.012     Document Type: Article
Times cited : (33)

References (48)
  • 2
    • 0032538307 scopus 로고    scopus 로고
    • A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis
    • J. Boisbouvier, J.P. Albrand, M. Blackledge, M. Jaquinod, H. Schweitz, and M. Lazdunski A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis J Mol Biol 283 1998 205 219
    • (1998) J Mol Biol , vol.283 , pp. 205-219
    • Boisbouvier, J.1    Albrand, J.P.2    Blackledge, M.3    Jaquinod, M.4    Schweitz, H.5    Lazdunski, M.6
  • 3
    • 0024844960 scopus 로고
    • Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II
    • P.E. Bougis, H. Rochat, and L.A. Smith Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II J Biol Chem 264 1989 19259 19265
    • (1989) J Biol Chem , vol.264 , pp. 19259-19265
    • Bougis, P.E.1    Rochat, H.2    Smith, L.A.3
  • 4
    • 0037394864 scopus 로고    scopus 로고
    • Granular gland transcriptomes in stimulated amphibian skin secretions
    • T. Chen, S. Farragher, A.J. Bjourson, D.F. Orr, P. Rao, and C. Shaw Granular gland transcriptomes in stimulated amphibian skin secretions Biochem J 371 2003 125 130
    • (2003) Biochem J , vol.371 , pp. 125-130
    • Chen, T.1    Farragher, S.2    Bjourson, A.J.3    Orr, D.F.4    Rao, P.5    Shaw, C.6
  • 5
    • 0037161808 scopus 로고    scopus 로고
    • Prokineticin 2 transmits the behavioral circadian rhythm of the suprachiasmatic nucleus
    • M.Y. Cheng, C.M. Bullock, C. Li, A.G. Lee, J.C. Bermak, and J. Belluzzi Prokineticin 2 transmits the behavioral circadian rhythm of the suprachiasmatic nucleus Nature 417 2002 405 410
    • (2002) Nature , vol.417 , pp. 405-410
    • Cheng, M.Y.1    Bullock, C.M.2    Li, C.3    Lee, A.G.4    Bermak, J.C.5    Belluzzi, J.6
  • 6
    • 0026756635 scopus 로고
    • Precursor structure of omega-conotoxin GVIA determined from a cDNA clone
    • C.J. Colledge, J.P. Hunsperger, J.S. Imperial, and D.R. Hillyard Precursor structure of omega-conotoxin GVIA determined from a cDNA clone Toxicon 30 1992 1111 1116
    • (1992) Toxicon , vol.30 , pp. 1111-1116
    • Colledge, C.J.1    Hunsperger, J.P.2    Imperial, J.S.3    Hillyard, D.R.4
  • 8
    • 0028172049 scopus 로고
    • On the site by which alpha-dendrotoxin binds to voltage-dependent potassium channels: Site-directed mutagenesis reveals that the lysine triplet 28-30 is not essential for binding
    • J.M. Danse, E.G. Rowan, S. Gasparini, F. Ducancel, H. Vatanpour, and L.C. Young On the site by which alpha-dendrotoxin binds to voltage-dependent potassium channels: site-directed mutagenesis reveals that the lysine triplet 28-30 is not essential for binding FEBS Lett 356 1994 153 158
    • (1994) FEBS Lett , vol.356 , pp. 153-158
    • Danse, J.M.1    Rowan, E.G.2    Gasparini, S.3    Ducancel, F.4    Vatanpour, H.5    Young, L.C.6
  • 9
    • 0027234680 scopus 로고
    • Sequence of the cDNA coding for the lethal neurotoxin Tx1 from the Brazilian "armed" spider Phoneutria nigriventer predicts the synthesis and processing of a preprotoxin
    • M.R. Diniz, M.J. Paine, C.R. Diniz, R.D. Theakston, and J.M. Crampton Sequence of the cDNA coding for the lethal neurotoxin Tx1 from the Brazilian "armed" spider Phoneutria nigriventer predicts the synthesis and processing of a preprotoxin J Biol Chem 268 1993 15340 15342
    • (1993) J Biol Chem , vol.268 , pp. 15340-15342
    • Diniz, M.R.1    Paine, M.J.2    Diniz, C.R.3    Theakston, R.D.4    Crampton, J.M.5
  • 10
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (delta-atracotoxin-Hv1): Implications for binding of site-3 toxins to the voltage-gated sodium channel
    • J.I. Fletcher, B.E. Chapman, J.P. Mackay, Howden MEH, and G.F. King The structure of versutoxin (delta-atracotoxin-Hv1): implications for binding of site-3 toxins to the voltage-gated sodium channel Structure 5 1997 1525 1535
    • (1997) Structure , vol.5 , pp. 1525-1535
    • Fletcher, J.I.1    Chapman, B.E.2    MacKay, J.P.3    Meh, H.4    King, G.F.5
  • 11
    • 0030981657 scopus 로고    scopus 로고
    • The structure of a novel insecticidal neurotoxin, ω-atracotoxin- HV1, from the venom of an Australian funnel web spider
    • J.I. Fletcher, R. Smith, S.I. O'Donoghue, M. Nilges, M. Connor, and M.E. Howden The structure of a novel insecticidal neurotoxin, ω-atracotoxin- HV1, from the venom of an Australian funnel web spider Nature Struct Biol 4 1997 559 566
    • (1997) Nature Struct Biol , vol.4 , pp. 559-566
    • Fletcher, J.I.1    Smith, R.2    O'Donoghue, S.I.3    Nilges, M.4    Connor, M.5    Howden, M.E.6
  • 12
    • 0033200207 scopus 로고    scopus 로고
    • High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide
    • J.I. Fletcher, A.J. Dingley, R. Smith, M. Connor, M.J. Christie, and G.F. King High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide Eur J Biochem 264 1999 525 533
    • (1999) Eur J Biochem , vol.264 , pp. 525-533
    • Fletcher, J.I.1    Dingley, A.J.2    Smith, R.3    Connor, M.4    Christie, M.J.5    King, G.F.6
  • 13
    • 0032556910 scopus 로고    scopus 로고
    • Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction
    • A. Glinka, W. Wu, H. Delius, A.P. Monaghan, C. Blumenstock, and C. Niehrs Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction Nature 391 1998 357 362
    • (1998) Nature , vol.391 , pp. 357-362
    • Glinka, A.1    Wu, W.2    Delius, H.3    Monaghan, A.P.4    Blumenstock, C.5    Niehrs, C.6
  • 14
    • 0033543156 scopus 로고    scopus 로고
    • Min-21 and min-23, the smallest peptides that fold like a cystine-stabilized beta-sheet motif: Design, solution structure, and thermal stability
    • A. Heitz, D. Le-Nguyen, and L. Chiche Min-21 and min-23, the smallest peptides that fold like a cystine-stabilized beta-sheet motif: design, solution structure, and thermal stability Biochemistry 38 1999 10615 10625
    • (1999) Biochemistry , vol.38 , pp. 10615-10625
    • Heitz, A.1    Le-Nguyen, D.2    Chiche, L.3
  • 15
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • E.G. Hutchinson, and J.M. Thornton PROMOTIF - a program to identify and analyze structural motifs in proteins Protein Sci 5 1996 212 220
    • (1996) Protein Sci , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 16
    • 0019122103 scopus 로고
    • Snake venom. the amino acid sequence of protein a from Dendroaspis polylepis polylepis (black mamba) venom
    • F.J. Joubert, and D.J. Strydom Snake venom. The amino acid sequence of protein A from Dendroaspis polylepis polylepis (black mamba) venom Hoppe Seylers Z Physiol Chem 361 1980 1787 1794
    • (1980) Hoppe Seylers Z Physiol Chem , vol.361 , pp. 1787-1794
    • Joubert, F.J.1    Strydom, D.J.2
  • 17
    • 0032403418 scopus 로고    scopus 로고
    • Cloning, cDNA sequence analysis and patch clamp studies of a toxin from the venom of the armed spider (Phoneutria nigriventer)
    • E. Kalapothakis, C.L. Penaforte, R.M. Leao, J.S. Cruz, V.F. Prado, and M.N. Cordeiro Cloning, cDNA sequence analysis and patch clamp studies of a toxin from the venom of the armed spider (Phoneutria nigriventer) Toxicon 36 1998 1971 1980
    • (1998) Toxicon , vol.36 , pp. 1971-1980
    • Kalapothakis, E.1    Penaforte, C.L.2    Leao, R.M.3    Cruz, J.S.4    Prado, V.F.5    Cordeiro, M.N.6
  • 18
    • 0032538802 scopus 로고    scopus 로고
    • Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): Implications for IGF and IGF-I receptor interactions
    • W. Kalus, M. Zweckstetter, C. Renner, Y. Sanchez, J. Georgescu, and M. Grol Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions EMBO J 17 1998 6558 6572
    • (1998) EMBO J , vol.17 , pp. 6558-6572
    • Kalus, W.1    Zweckstetter, M.2    Renner, C.3    Sanchez, Y.4    Georgescu, J.5    Grol, M.6
  • 20
    • 0018846710 scopus 로고
    • Prepromelittin: Specific cleavage of the pre- and the propeptide in vitro
    • G. Kreil, C. Mollay, R. Kaschnitz, L. Haiml, and U. Vilas Prepromelittin: specific cleavage of the pre- and the propeptide in vitro Ann N Y Acad Sci 343 1980 338 346
    • (1980) Ann N Y Acad Sci , vol.343 , pp. 338-346
    • Kreil, G.1    Mollay, C.2    Kaschnitz, R.3    Haiml, L.4    Vilas, U.5
  • 21
    • 0037333793 scopus 로고    scopus 로고
    • Two novel Bv8-like peptides from skin secretions of the toad Bombina maxima
    • R. Lai, H. Liu, W.H. Lee, and Y. Zhang Two novel Bv8-like peptides from skin secretions of the toad Bombina maxima Comp Biochem Physiol B: Biochem Mol Biol 134 2003 509 514
    • (2003) Comp Biochem Physiol B: Biochem Mol Biol , vol.134 , pp. 509-514
    • Lai, R.1    Liu, H.2    Lee, W.H.3    Zhang, Y.4
  • 22
    • 0035974803 scopus 로고    scopus 로고
    • Identification of an angiogenic mitogen selective for endocrine gland endothelium
    • J. LeCouter, J. Kowalski, J. Foster, P. Hass, Z. Zhang, and L. Dillard-Telm Identification of an angiogenic mitogen selective for endocrine gland endothelium Nature 412 2001 877 884
    • (2001) Nature , vol.412 , pp. 877-884
    • Lecouter, J.1    Kowalski, J.2    Foster, J.3    Hass, P.4    Zhang, Z.5    Dillard-Telm, L.6
  • 23
    • 0036445595 scopus 로고    scopus 로고
    • EG-VEGF and the concept of tissue-specific angiogenic growth factors
    • J. LeCouter, and N. Ferrara EG-VEGF and the concept of tissue-specific angiogenic growth factors Semin Cell Dev Biol 13 2002 3 8
    • (2002) Semin Cell Dev Biol , vol.13 , pp. 3-8
    • Lecouter, J.1    Ferrara, N.2
  • 24
    • 0038801356 scopus 로고    scopus 로고
    • The role of EG-VEGF in the regulation of angiogenesis in endocrine glands
    • J. LeCouter, R. Lin, and N. Ferrara The role of EG-VEGF in the regulation of angiogenesis in endocrine glands Cold Spring Harb Symp Quant Biol 67 2002 217 221
    • (2002) Cold Spring Harb Symp Quant Biol , vol.67 , pp. 217-221
    • Lecouter, J.1    Lin, R.2    Ferrara, N.3
  • 25
    • 0036732411 scopus 로고    scopus 로고
    • Endocrine gland-derived VEGF and the emerging hypothesis of organ-specific regulation of angiogenesis
    • J. LeCouter, R. Lin, and N. Ferrara Endocrine gland-derived VEGF and the emerging hypothesis of organ-specific regulation of angiogenesis Nat Med 8 2002 913 917
    • (2002) Nat Med , vol.8 , pp. 913-917
    • Lecouter, J.1    Lin, R.2    Ferrara, N.3
  • 26
    • 0038183983 scopus 로고    scopus 로고
    • Mouse endocrine gland-derived vascular endothelial growth factor: A distinct expression pattern from its human ortholog suggests different roles as a regulator of organ-specific angiogenesis
    • J. LeCouter, R. Lin, G. Frantz, Z. Zhang, K. Hillan, and N. Ferrara Mouse endocrine gland-derived vascular endothelial growth factor: a distinct expression pattern from its human ortholog suggests different roles as a regulator of organ-specific angiogenesis Endocrinology 144 2003 2606 2616
    • (2003) Endocrinology , vol.144 , pp. 2606-2616
    • Lecouter, J.1    Lin, R.2    Frantz, G.3    Zhang, Z.4    Hillan, K.5    Ferrara, N.6
  • 27
    • 0035064732 scopus 로고    scopus 로고
    • Identification of two prokineticin cDNAs: Recombinant proteins potently contract gastrointestinal smooth muscle
    • M. Li, C.M. Bullock, D.J. Knauer, F.J. Ehlert, and Q.Y. Zhou Identification of two prokineticin cDNAs: recombinant proteins potently contract gastrointestinal smooth muscle Mol Pharmacol 59 2001 692 698
    • (2001) Mol Pharmacol , vol.59 , pp. 692-698
    • Li, M.1    Bullock, C.M.2    Knauer, D.J.3    Ehlert, F.J.4    Zhou, Q.Y.5
  • 28
    • 0037205491 scopus 로고    scopus 로고
    • Identification and molecular characterization of two closely related G protein-coupled receptors activated by prokineticins/endocrine gland vascular endothelial growth factor
    • D.C. Lin, C.M. Bullock, F.J. Ehlert, J.L. Chen, H. Tian, and Q.Y. Zhou Identification and molecular characterization of two closely related G protein-coupled receptors activated by prokineticins/endocrine gland vascular endothelial growth factor J Biol Chem 277 2002 19276 19280
    • (2002) J Biol Chem , vol.277 , pp. 19276-19280
    • Lin, D.C.1    Bullock, C.M.2    Ehlert, F.J.3    Chen, J.L.4    Tian, H.5    Zhou, Q.Y.6
  • 29
    • 0036294227 scopus 로고    scopus 로고
    • Isolation and identification of EG-VEGF/prokineticins as cognate ligands for two orphan G-protein-coupled receptors
    • Y. Masuda, Y. Takatsu, Y. Terao, S. Kumano, Y. Ishibashi, and M. Suenaga Isolation and identification of EG-VEGF/prokineticins as cognate ligands for two orphan G-protein-coupled receptors Biochem Biophys Res Commun 293 2002 396 402
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 396-402
    • Masuda, Y.1    Takatsu, Y.2    Terao, Y.3    Kumano, S.4    Ishibashi, Y.5    Suenaga, M.6
  • 30
    • 0031059284 scopus 로고    scopus 로고
    • Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei
    • M.L. Mattinen, M. Kontteli, J. Kerovuo, M. Linder, A. Annila, and G. Lindeberg Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei Protein Sci 6 1997 294 303
    • (1997) Protein Sci , vol.6 , pp. 294-303
    • Mattinen, M.L.1    Kontteli, M.2    Kerovuo, J.3    Linder, M.4    Annila, A.5    Lindeberg, G.6
  • 31
    • 17744392200 scopus 로고    scopus 로고
    • The mammalian homologue of the novel peptide Bv8 is expressed in the central nervous system and supports neuronal survival by activating the MAP kinase/PI-3-kinase pathways
    • D. Melchiorri, V. Bruno, G. Besong, R.T. Ngomba, L. Cuomo, and A. De Blasi The mammalian homologue of the novel peptide Bv8 is expressed in the central nervous system and supports neuronal survival by activating the MAP kinase/PI-3-kinase pathways Eur J Neurosci 13 2001 1694 1702
    • (2001) Eur J Neurosci , vol.13 , pp. 1694-1702
    • Melchiorri, D.1    Bruno, V.2    Besong, G.3    Ngomba, R.T.4    Cuomo, L.5    De Blasi, A.6
  • 32
    • 0033033979 scopus 로고    scopus 로고
    • Bv8, a small protein from frog skin and its homologue from snake venom induce hyperalgesia in rats
    • C. Mollay, C. Wechselberger, G. Mignogna, L. Negri, P. Melchiorri, and D. Barra Bv8, a small protein from frog skin and its homologue from snake venom induce hyperalgesia in rats Eur J Pharmacol 374 1999 189 196
    • (1999) Eur J Pharmacol , vol.374 , pp. 189-196
    • Mollay, C.1    Wechselberger, C.2    Mignogna, G.3    Negri, L.4    Melchiorri, P.5    Barra, D.6
  • 35
    • 1942438958 scopus 로고    scopus 로고
    • Structure and function of δ-atracotoxins: Lethal neurotoxins targeting the voltage-gated sodium channel
    • G.M. Nicholson, M. Little, and L.C. Birinyi-Strachan Structure and function of δ-atracotoxins: lethal neurotoxins targeting the voltage-gated sodium channel Toxicon 43 2004 587 599
    • (2004) Toxicon , vol.43 , pp. 587-599
    • Nicholson, G.M.1    Little, M.2    Birinyi-Strachan, L.C.3
  • 36
    • 0029986992 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities
    • D.O. Omecinsky, K.E. Holub, M.E. Adams, and M.D. Reily Three-dimensional structure analysis of μ-agatoxins: further evidence for common motifs among neurotoxins with diverse ion channel specificities Biochemistry 35 1996 2836 2844
    • (1996) Biochemistry , vol.35 , pp. 2836-2844
    • Omecinsky, D.O.1    Holub, K.E.2    Adams, M.E.3    Reily, M.D.4
  • 37
    • 0029032454 scopus 로고
    • The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the alpha-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae)
    • M. Pescatori, A. Bradbury, F. Bouet, N. Gargano, A. Mastrogiacomo, and A. Grasso The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the alpha-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae) Eur J Biochem 230 1995 322 328
    • (1995) Eur J Biochem , vol.230 , pp. 322-328
    • Pescatori, M.1    Bradbury, A.2    Bouet, F.3    Gargano, N.4    Mastrogiacomo, A.5    Grasso, A.6
  • 38
    • 0023042278 scopus 로고
    • The processing of peptide precursors Proline-directed arginyl cleavage' and other monobasic processing mechanisms
    • T.W. Schwartz The processing of peptide precursors Proline-directed arginyl cleavage' and other monobasic processing mechanisms FEBS Lett 200 1986 1 10
    • (1986) FEBS Lett , vol.200 , pp. 1-10
    • Schwartz, T.W.1
  • 39
    • 0032742094 scopus 로고    scopus 로고
    • MIT1, a black mamba toxin with a new and highly potent activity on intestinal contraction
    • H. Schweitz, P. Pacaud, S. Diochot, D. Moinier, and M. Lazdunski MIT1, a black mamba toxin with a new and highly potent activity on intestinal contraction FEBS Lett 461 1999 183 188
    • (1999) FEBS Lett , vol.461 , pp. 183-188
    • Schweitz, H.1    Pacaud, P.2    Diochot, S.3    Moinier, D.4    Lazdunski, M.5
  • 40
    • 0036147845 scopus 로고    scopus 로고
    • The structure of spider toxin huwentoxin-II with unique disulfide linkage: Evidence for structural evolution
    • Q. Shu, S.Y. Lu, X.C. Gu, and S.P. Liang The structure of spider toxin huwentoxin-II with unique disulfide linkage: evidence for structural evolution Protein Sci 11 2002 245 252
    • (2002) Protein Sci , vol.11 , pp. 245-252
    • Shu, Q.1    Lu, S.Y.2    Gu, X.C.3    Liang, S.P.4
  • 42
    • 0033991706 scopus 로고    scopus 로고
    • Isolation of a funnel web spider polypeptide with homology to mamba intestinal toxin 1 and the embryonic head inducer Dickkopf1
    • T.H. Szeto, X-H. Wang, R. Smith, M. Connor, M.J. Christie, and G.M. Nicholson Isolation of a funnel web spider polypeptide with homology to mamba intestinal toxin 1 and the embryonic head inducer Dickkopf1 Toxicon 38 2000 429 442
    • (2000) Toxicon , vol.38 , pp. 429-442
    • Szeto, T.H.1    Wang, X.-H.2    Smith, R.3    Connor, M.4    Christie, M.J.5    Nicholson, G.M.6
  • 43
    • 1942534974 scopus 로고    scopus 로고
    • Australian funnel-web spiders: Master insecticide chemists
    • H.W. Tedford, F. Maggio, B.L. Sollod, and G.F. King Australian funnel-web spiders: master insecticide chemists Toxicon 43 2004 601 618
    • (2004) Toxicon , vol.43 , pp. 601-618
    • Tedford, H.W.1    Maggio, F.2    Sollod, B.L.3    King, G.F.4
  • 45
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-procolipase complex
    • H. van Tilbeurgh, L. Sarda, R. Verger, and C. Cambillau Structure of the pancreatic lipase-procolipase complex Nature 359 1992 159 162
    • (1992) Nature , vol.359 , pp. 159-162
    • Van Tilbeurgh, H.1    Sarda, L.2    Verger, R.3    Cambillau, C.4
  • 46
    • 0033593549 scopus 로고    scopus 로고
    • Divergence time estimates for the early history of animal phyla and the origin of plants, animals and fungi
    • D.Y. Wang, S. Kumar, and S.B. Hedges Divergence time estimates for the early history of animal phyla and the origin of plants, animals and fungi Proc R Soc London B: Biol Sci 266 1999 163 171
    • (1999) Proc R Soc London B: Biol Sci , vol.266 , pp. 163-171
    • Wang, D.Y.1    Kumar, S.2    Hedges, S.B.3
  • 47
    • 0034043512 scopus 로고    scopus 로고
    • Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge
    • X-H. Wang, M. Connor, R. Smith, M.W. Maciejewski, Howden MEH, and G.M. Nicholson Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge Nat Struct Biol 7 2000 505 513
    • (2000) Nat Struct Biol , vol.7 , pp. 505-513
    • Wang, X.-H.1    Connor, M.2    Smith, R.3    MacIejewski, M.W.4    Meh, H.5    Nicholson, G.M.6


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